ID A0A7K6X1Z9_9PASE Unreviewed; 888 AA.
AC A0A7K6X1Z9;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN Name=Znf598 {ECO:0000313|EMBL:NWX53318.1};
GN ORFNames=PROCAF_R05514 {ECO:0000313|EMBL:NWX53318.1};
OS Promerops cafer (Cape sugarbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Nectariniidae; Promerops.
OX NCBI_TaxID=254652 {ECO:0000313|EMBL:NWX53318.1, ECO:0000313|Proteomes:UP000587587};
RN [1] {ECO:0000313|EMBL:NWX53318.1, ECO:0000313|Proteomes:UP000587587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-UC-030-53 {ECO:0000313|EMBL:NWX53318.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NWX53318.1}.
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DR EMBL; VZSE01000016; NWX53318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K6X1Z9; -.
DR Proteomes; UP000587587; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:TreeGrafter.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR InterPro; IPR057634; PAH_ZNF598/HEL2.
DR InterPro; IPR041888; RING-HC_ZNF598/HEL2.
DR InterPro; IPR044288; ZNF598/HEL2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR059042; Znf_C2H2_ZNF598.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF23202; PAH_ZNF598; 1.
DR Pfam; PF25447; RING_ZNF598; 1.
DR Pfam; PF23208; zf_C2H2_ZNF598; 1.
DR SMART; SM00355; ZnF_C2H2; 5.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:NWX53318.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000587587};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 7..47
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 294..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..313
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..337
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWX53318.1"
FT NON_TER 888
FT /evidence="ECO:0000313|EMBL:NWX53318.1"
SQ SEQUENCE 888 AA; 99105 MW; DCABE0F7F5209FB1 CRC64;
GPAEGPCVLC CGELDVVALG RCEHPICYRC SVRMRALCGV RYCAVCREEL RQVVFGRKLP
SFSSIALHQL QHEKKYDIYF MDAEVYALYR KLLQHECSLC PDAKPFNTFA DLEQHMRKQH
ELFCCKLCVK HLKIFTYERK WYSRKDLARH RIHGDPDDTS HRGHPLCKFC DERYLDNDEL
LKHLRRDHYF CHFCDSEGAQ DSVFSLPSDY EYLREHFREK HFLCEEGRCS SEQFTHAFRT
EIDYKAHKSA CHSKSRAEAR QNRHIDLQFT YAPRHPRRSD GVVSAEDYEE VDRFNRQGRA
GRLSSRGSQQ NRRGSWRYKR EEEDRDVAAA VRASVAAKRQ EEKKRVEDKE EGSSSRGRKE
DLRDPDALGS KRVPKSSNDV TGECWTGPAA AGHLSVWKVP SETAANGALS QDDFPAIGSA
AGPLQGSAQP ALVKLKEEDF PSLSSSAAPT ISSGMSLTYT ATARKAAFQE EDFPALVSKV
KPTNRTVTHI TSAWNNGSSK NVVKAMSSPC VNQPAKKPSL NTSKGSKKSN KLCESDDEDG
GGGLTTQEIR NTPTMFDVSS LLAASTSQTF TKVGRKKKMG VEKQSPSSPR PSQETPLPRP
ATEKPPEAEQ PCRVFPAAHG PDRATAVVNG HSEKPSAGCA TPKEPPGLKK PPVTNKCPLP
QEDFPALGSS GSARMPPPPG FNSVVLLKNP PPPPGLSVPV SKPPPGFAVI PSSTISEPVT
TALKEPKSCH GSYLIPENFQ QRNIQLIQSI KEFLQSDESK FNKFKTHSGQ FRQGLISAAQ
YYKSCRELLG ENFKKIFKEL LVLLPDTAKQ QELLSAHNDF RIKEKQSSNK PKKNKKNVWQ
TDSPADLDCS VCPTCRQVLT QQDVVTHKAL HIEDEEFPSL QAISRIIS
//
